Journal article icon

Journal article

Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure

Abstract:

Intrinsically disordered proteins (IDPs) are characterized by a lack of defined structure. Instead, they populate ensembles of rapidly interconverting conformations with marginal structural stabilities. Changes in solution conditions such as temperature and crowding agents consequently affect IDPs more than their folded counterparts. Here we reveal that the residual structure content of IDPs is modulated both by ionic strength and by the type of ions present in solution. We show that these io...

Expand abstract
Publication status:
Published
Peer review status:
Peer reviewed
Version:
Accepted Manuscript

Actions


Access Document


Files:
Publisher copy:
10.1073/pnas.1705105114

Authors


More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
Cambridge Trust More from this funder
Publisher:
National Academy of Sciences Publisher's website
Journal:
Proceedings of the National Academy of Sciences Journal website
Volume:
114
Issue:
37
Pages:
9882-9887
Publication date:
2017-08-28
Acceptance date:
2017-08-01
DOI:
ISSN:
0027-8424 and 1091-6490
Pubs id:
pubs:867846
URN:
uri:d7d7aafd-5069-432b-8824-acdd031bb15f
UUID:
uuid:d7d7aafd-5069-432b-8824-acdd031bb15f
Local pid:
pubs:867846

Terms of use


Metrics


Views and Downloads






If you are the owner of this record, you can report an update to it here: Report update to this record

TO TOP